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[[Image:2bvp.gif|left|200px]]<br />
[[Image:2bvp.gif|left|200px]]<br /><applet load="2bvp" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="2bvp" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="2bvp, resolution 1.35&Aring;" />
caption="2bvp, resolution 1.35&Aring;" />
'''STRUCTURES OF THREE HIV-1 HLA-B5703-PEPTIDE COMPLEXES AND IDENTIFICATION OF RELATED HLAS POTENTIALLY ASSOCIATED WITH LONG-TERM NON-PROGRESSION'''<br />
'''STRUCTURES OF THREE HIV-1 HLA-B5703-PEPTIDE COMPLEXES AND IDENTIFICATION OF RELATED HLAS POTENTIALLY ASSOCIATED WITH LONG-TERM NON-PROGRESSION'''<br />


==Overview==
==Overview==
Long-term nonprogression during acute HIV infection has been strongly, associated with HLA-B*5701 or HLA-B*5703. In this study, we present the, high resolution crystal structures of HLA-B*5703 complexes with three, HIV-1 epitopes: ISPRTLNAW (ISP), KAFSPEVIPMF (KAF-11), and KAFSPEVI, (KAF-8). These reveal peptide anchoring at position 2 and their C termini., The different peptide lengths and primary sequences are accommodated by, variation in the specific contacts made to the HLA-B*5703, flexibility in, water structure, and conformational adjustment of side chains within the, peptide-binding groove. The peptides adopt markedly different, conformations, and trap variable numbers of water molecules, near a, cluster of tyrosine side chains located in the central region of the, peptide-binding groove. The KAF-11 epitope completely encompasses the, shorter KAF-8 epitope but the peptides are presented in different, conformations; the KAF-11 peptide arches out of the peptide-binding, groove, exposing a significant main chain surface area. Bioinformatic, analysis of the MHC side chains observed to contribute to the peptide, anchor specificity, and other specific peptide contacts, reveals HLA, alleles associated with long-term nonprogression and a number of related, HLA alleles that may share overlapping peptide repertoires with HLA-B*5703, and thus may display a similar capacity for efficient immune control of, HIV-1 infection.
Long-term nonprogression during acute HIV infection has been strongly associated with HLA-B*5701 or HLA-B*5703. In this study, we present the high resolution crystal structures of HLA-B*5703 complexes with three HIV-1 epitopes: ISPRTLNAW (ISP), KAFSPEVIPMF (KAF-11), and KAFSPEVI (KAF-8). These reveal peptide anchoring at position 2 and their C termini. The different peptide lengths and primary sequences are accommodated by variation in the specific contacts made to the HLA-B*5703, flexibility in water structure, and conformational adjustment of side chains within the peptide-binding groove. The peptides adopt markedly different conformations, and trap variable numbers of water molecules, near a cluster of tyrosine side chains located in the central region of the peptide-binding groove. The KAF-11 epitope completely encompasses the shorter KAF-8 epitope but the peptides are presented in different conformations; the KAF-11 peptide arches out of the peptide-binding groove, exposing a significant main chain surface area. Bioinformatic analysis of the MHC side chains observed to contribute to the peptide anchor specificity, and other specific peptide contacts, reveals HLA alleles associated with long-term nonprogression and a number of related HLA alleles that may share overlapping peptide repertoires with HLA-B*5703 and thus may display a similar capacity for efficient immune control of HIV-1 infection.


==Disease==
==Disease==
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==About this Structure==
==About this Structure==
2BVP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BVP OCA].  
2BVP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BVP OCA].  


==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Gillespie, G.]]
[[Category: Gillespie, G.]]
[[Category: Jones, E.Y.]]
[[Category: Jones, E Y.]]
[[Category: Kaul, R.]]
[[Category: Kaul, R.]]
[[Category: Mcmichael, A.J.]]
[[Category: Mcmichael, A J.]]
[[Category: Overton, I.M.]]
[[Category: Overton, I M.]]
[[Category: Roche, P.]]
[[Category: Roche, P.]]
[[Category: Rowland-Jones, S.]]
[[Category: Rowland-Jones, S.]]
[[Category: Stewart-Jones, G.B.]]
[[Category: Stewart-Jones, G B.]]
[[Category: glycoprotein]]
[[Category: glycoprotein]]
[[Category: glycoprotein/peptide complex]]
[[Category: glycoprotein/peptide complex]]
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[[Category: transmembrane]]
[[Category: transmembrane]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:06:51 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:42:08 2008''

Revision as of 17:42, 21 February 2008

File:2bvp.gif


2bvp, resolution 1.35Å

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STRUCTURES OF THREE HIV-1 HLA-B5703-PEPTIDE COMPLEXES AND IDENTIFICATION OF RELATED HLAS POTENTIALLY ASSOCIATED WITH LONG-TERM NON-PROGRESSION

OverviewOverview

Long-term nonprogression during acute HIV infection has been strongly associated with HLA-B*5701 or HLA-B*5703. In this study, we present the high resolution crystal structures of HLA-B*5703 complexes with three HIV-1 epitopes: ISPRTLNAW (ISP), KAFSPEVIPMF (KAF-11), and KAFSPEVI (KAF-8). These reveal peptide anchoring at position 2 and their C termini. The different peptide lengths and primary sequences are accommodated by variation in the specific contacts made to the HLA-B*5703, flexibility in water structure, and conformational adjustment of side chains within the peptide-binding groove. The peptides adopt markedly different conformations, and trap variable numbers of water molecules, near a cluster of tyrosine side chains located in the central region of the peptide-binding groove. The KAF-11 epitope completely encompasses the shorter KAF-8 epitope but the peptides are presented in different conformations; the KAF-11 peptide arches out of the peptide-binding groove, exposing a significant main chain surface area. Bioinformatic analysis of the MHC side chains observed to contribute to the peptide anchor specificity, and other specific peptide contacts, reveals HLA alleles associated with long-term nonprogression and a number of related HLA alleles that may share overlapping peptide repertoires with HLA-B*5703 and thus may display a similar capacity for efficient immune control of HIV-1 infection.

DiseaseDisease

Known diseases associated with this structure: Abacavir hypersensitivity, susceptibility to OMIM:[142830], Spondyloarthropathy, susceptibility to, 1 OMIM:[142830], Stevens-Johnson syndrome, carbamazepine-induced, susceptibility to OMIM:[142830]

About this StructureAbout this Structure

2BVP is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structures of three HIV-1 HLA-B*5703-peptide complexes and identification of related HLAs potentially associated with long-term nonprogression., Stewart-Jones GB, Gillespie G, Overton IM, Kaul R, Roche P, McMichael AJ, Rowland-Jones S, Jones EY, J Immunol. 2005 Aug 15;175(4):2459-68. PMID:16081817

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